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  QH*- Ubisemiquinone Radical in the bo3-Type Ubiquinol Oxidase Studied by Pulsed Electron Paramagnetic Resonance and Hyperfine Sublevel Correlation Spectroscopy

Grimaldi, S., MacMillan, F., Ostermann, T., Ludwig, B., Michel, H., & Prisner, T. (2001). QH*- Ubisemiquinone Radical in the bo3-Type Ubiquinol Oxidase Studied by Pulsed Electron Paramagnetic Resonance and Hyperfine Sublevel Correlation Spectroscopy. Biochemistry, 40(4), 1037-1043. doi:10.1021/bi001641+.

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 Creators:
Grimaldi, Stéphane1, Author
MacMillan, Fraser1, Author
Ostermann, Thomas2, 3, Author           
Ludwig, Bernd3, Author
Michel, Hartmut2, Author                 
Prisner, Thomas1, Author
Affiliations:
1Institut für Physikalische und Theoretische Chemie, J. W. Goethe Universität Frankfurt, 60439 Frankfurt am Main, Germany, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Institut für Biochemie, J. W. Goethe Universität Frankfurt, 60439 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: Peptides and proteins; Quinones; Electron paramagnetic resonance spectroscopy; Nitrogen; Screening assays
 Abstract: The high-affinity QH ubiquinone-binding site in the bo3 ubiquinol oxidase from Escherichia coli has been characterized by an investigation of the native ubiquinone radical anion QH*- by pulsed electron paramagnetic resonance (EPR) spectroscopy. One- and two-dimensional electron spin−echo envelope modulation (ESEEM) spectra reveal strong interactions of the unpaired electron of QH*- with a nitrogen nucleus from the surrounding protein matrix. From analysis of the experimental data, the 14N nuclear quadrupolar parameters have been determined:  κ = e2qQ/4h = 0.93 MHz and η = 0.50. This assignment is confirmed by hyperfine sublevel correlation (HYSCORE) spectroscopy. On the basis of a comparison of these data with those obtained previously for other membrane-protein bound semiquinone radicals and model systems, this nucleus is assigned to a protein backbone nitrogen. This result is discussed with regard to the location and potential function of QH in the enzyme.

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Language(s): eng - English
 Dates: 2000-10-062000-07-132001-01-062001-01-01
 Publication Status: Issued
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/bi001641+
 Degree: -

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Title: Biochemistry
Source Genre: Journal
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Publ. Info: Columbus, Ohio : American Chemical Society
Pages: - Volume / Issue: 40 (4) Sequence Number: - Start / End Page: 1037 - 1043 Identifier: ISSN: 0006-2960
CoNE: https://pure.mpg.de/cone/journals/resource/954925384103